Search by BoMiProt ID - Bomi68


Primary Information

BoMiProt ID Bomi68
Protein Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
Organism Bos taurus
Uniprot IdP10894
Milk FractionWhey, Exosome
Ref Sequence Id NP_777242.1
Amino Acid Lenth 1216
Molecular Weight 138715
Fasta Sequence https://www.uniprot.org/uniprot/P10894.fasta
Gene Name PLCB1
Gene Id 287026
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function class of phospholipases that cleaves phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond producing DAGs and phosphomonoesters; constitutes an important step in the inositide signaling pathways; plays an important role in brain function and is thus associated with brain disorders; it regulates both cortical development and synaptic plasticity; participate in the differentiation and activation of immune cells that control both the innate and adaptive immune systems; linked to the development of myeloproliferative neoplasm in mice; specifi c key role in cell migration and invasion, therefore contributing to carcinogenesis
Biochemical Properties calcium (Ca2+)-dependent phosphodiesterases; PI-PLCß enzymes are usually activated by G protein-coupled receptors; PI-PLCγ subtypes are commonly activated by receptor tyrosine kinase (RTK), via SH2 domain-phospho-tyrosine interaction; Most of PI-PLCß may have a high guanosine; triphosphatase activating protein (GAP) activity
Significance in milk responsible for the hydrolyses of phospholipids of the MFG membrane, thereby affecting the stability of the cream emulsion;
Additional Comments 13 mammalian PLC isozymes identified so far are organized within 6 families: β(1–4), γ(1–2), δ(1,3,4), ε, ζ and η(1–2); phospholipase treatment of milk was found to reduce fat losses in whey and cooking water and to increase CY by improving fat and moisture retention in the cheese curd in Mozzarella cheese
Bibliography 1. Xiao, W., Hong, H., Kawakami, Y., Kato, Y., Wu, D., Yasudo, H., … Kawakami, T. (2009). Tumor suppression by phospholipase C-beta3 via SHP-1-mediated dephosphorylation of Stat5. Cancer Cell, 16(2), 161–171. https://doi.org/10.1016/j.ccr.2009.05.018.
2. Lin, X. H., Kitamura, N., Hashimoto, T., Shirakawa, O., & Maeda, K. (1999). Opposite changes in phosphoinositide-specific phospholipase C immunoreactivity in the left prefrontal and superior temporal cortex of patients with chronic schizophrenia. Biological Psychiatry, 46(12), 1665–1671. https://doi.org/10.1016/s0006-3223(99)00036-0.
3. Koh, H.-Y. (2013). Phospholipase C-β1 and schizophrenia-related behaviors. Advances in Biological Regulation, 53(3), 242–248. https://doi.org/10.1016/j.jbior.2013.08.002.
4. Ross, E. M., Mateu, D., Gomes, A. V, Arana, C., Tran, T., & Litosch, I. (2006). Structural determinants for phosphatidic acid regulation of phospholipase C-beta1. The Journal of Biological Chemistry, 281(44), 33087–33094. https://doi.org/10.1074/jbc.M606487200.
5. Poli, A., Mongiorgi, S., Cocco, L., & Follo, M. Y. (2014). Protein kinase C involvement in cell cycle modulation. Biochemical Society Transactions, 42(5), 1471–1476. https://doi.org/10.1042/BST20140128.
6. Béziau, D. M., Toussaint, F., Blanchette, A., Dayeh, N. R., Charbel, C., Tardif, J. C., … Ledoux, J. (2015). Expression of Phosphoinositide-Specific Phospholipase C Isoforms in Native Endothelial Cells. PLoS ONE, 10(4). https://doi.org/10.1371/journal.pone.0123769.
7. Dadousis, C., Pegolo, S., Rosa, G. J. M., Gianola, D., Bittante, G., & Cecchinato, A. (2017). Pathway-based genome-wide association analysis of milk coagulation properties, curd firmness, cheese yield, and curd nutrient recovery in dairy cattle. Journal of Dairy Science, 100(2), 1223–1231. https://doi.org/10.3168/jds.2016-11587.